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COVID-19 series: Dr. Kurt Haas receives CIHR grant to study the role of receptor gene ACE2
In the coming weeks, we will be profiling COVID-19 work and expertise from Djavad Mowafaghian Centre for Brain Health members. In this story we profile DMCBH researcher Dr. Kurt Haas, Professor in the Department of Cellular and Physiological Sciences, who received a CIHR grant last week to support his COVID-19 research.
The main focus of the Haas lab has been to better understand autism, by studying how single nucleotide polymorphisms—substitutions of one nucleotide in the genome—change protein function in autism-associated genes.
But when COVID-19 hit North America in March, the team realized they could apply their research process to studying the virus. The Haas lab began studying the gene ACE2, which makes a protein that acts as a receptor and binds the COVID-19 virus on the surface of cells lining the lung.
“We realized that one of the big questions in this pandemic is why people have such different expression of the disease, ranging from no symptoms at all to life threatening pneumonia,” says Dr. Kurt Haas (pictured), DMCBH researcher and Professor in the Department of Cellular and Physiological Sciences. “One reason why this is happening may be due to variants of the ACE2 gene, which is why we want to study it.”
Dr. Haas’ team has been working on this around the clock since the outbreak happened, and last week he secured CIHR funding to support the project for the next year. His lab will be making all possible mutations of the ACE2 gene and testing how each variant binds to the viral protein.
There are two main goals of this research. The first, is to gain a better understanding of the role ACE2 plays in how severely the virus infects a person. The second, is to use this research to aid in the development of new therapies. By better understanding ACE2’s function, new drugs could be designed that would block the virus from binding to it. But there’s a second aspect to how this work could help with therapies.
“We’re trying to identify versions of ACE2 that have heightened binding to the virus protein,” explains Dr. Haas. “This is very important because research from my colleague Dr. Josef Penninger has shown that the soluble form of ACE2 can be used as a sponge to bind and eradicate the virus, so our findings could help optimize his study.”
Dr. Haas says his lab has been creating ACE2 mutations and designing assays that will soon be tested. Their goal is to make large libraries of ACE2 mutants and to screen the impact of genetic variation on multiple aspects of ACE2 protein function.
“The implications of this work are relevant now but could also be very important in the future,” says Dr. Haas. “Once this platform is established, we can use it to study any new virus that appears that infects cells by binding the ACE2 receptor.”